2-hydroxyisoflavanone dehydratase
Class of enzymes
From Wikipedia, the free encyclopedia
The enzyme 2-hydroxyisoflavanone dehydratase (EC 4.2.1.105) catalyzes the chemical reaction
| 2-hydroxyisoflavanone dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.1.105 | ||||||||
| CAS no. | 56022-25-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 2,7,4′-trihydroxyisoflavanone hydro-lyase (daidzein-forming). This enzyme is also called 2,7,4′-trihydroxyisoflavanone hydro-lyase.[1] This enzyme forms part of the pathway to isoflavones from flavonoids.[2][3] The starting material, 2,4',7-trihydroxyisoflavanone, is produced from liquiritigenin by the enzyme isoflavonoid synthase[4]
2-hydroxyisoflavanone dehydratase also acts on the intermediate tetrahydroxyisoflavanone produced from naringenin, leading to genistein.[5]
The variant GmHID1 from Glycine max shows both these activities.[5].
